کاویئولین ۱

CAV1
معین‌کننده‌ها
نام‌های دیگر	CAV1, BSCL3, CGL3, LCCNS, MSTP085, PPH3, VIP21, Caveolin 1
شناسه‌های بیرونی	OMIM: 601047 MGI: 102709 HomoloGene: 1330 GeneCards: CAV1
موقعیت ژن (موش)
کروموزوم	کروموزوم ۶ (موش)
پایان	17,341,451 bp
الگوی گسترش RNA
	; ;
	More reference expression data
هستی‌شناسی ژن
عملکرد ملکولی	• protein-macromolecule adaptor activity; • transmembrane transporter binding; • structural molecule activity; • signaling receptor binding; • nitric-oxide synthase binding; • patched binding; • enzyme binding; • peptidase activator activity; • GO:0001948، GO:0016582 پیوند پروتئینی; • GO:0032947 molecular adaptor activity; • protein kinase binding; • ATPase binding; • cholesterol binding; • inward rectifier potassium channel inhibitor activity; • identical protein binding; • protein heterodimerization activity; • GO:0032403 protein-containing complex binding;
ترکیبات سلولی	• endocytic vesicle membrane; • اندوزوم; • membrane; • focal adhesion; • VCP-NPL4-UFD1 AAA ATPase complex; • perinuclear region of cytoplasm; • حفره غشایی; • مژک; • apical plasma membrane; • شبکه آندوپلاسمی; • لیپید رفت; • integral component of membrane; • دستگاه گلژی; • early endosome membrane; • پوسته یاخته; • intracellular anatomical structure; • cell cortex; • endoplasmic reticulum membrane; • Golgi membrane; • integral component of plasma membrane; • acrosomal membrane; • basolateral plasma membrane; • GO:0016023 cytoplasmic vesicle; • lipid droplet; • سیتوپلاسم; • GO:0009327 protein-containing complex; • سارکولما;
فرایند زیستی	• caveolin-mediated endocytosis; • positive regulation of calcium ion transport into cytosol; • انقباض عروق; • response to progesterone; • negative regulation of protein binding; • regulation of peptidase activity; • protein localization to plasma membrane raft; • mammary gland development; • vasculogenesis; • negative regulation of pinocytosis; • پاسخ به ایسکمی; • رگ‌زایی; • apoptotic signaling pathway; • positive regulation of extrinsic apoptotic signaling pathway; • cholesterol homeostasis; • triglyceride metabolic process; • negative regulation of canonical Wnt signaling pathway; • calcium ion transport; • negative regulation of cell population proliferation; • cellular response to transforming growth factor beta stimulus; • positive regulation of toll-like receptor 3 signaling pathway; • regulation of cytosolic calcium ion concentration; • regulation of smooth muscle contraction; • vesicle organization; • negative regulation of peptidyl-tyrosine autophosphorylation; • regulation of cardiac muscle cell action potential involved in regulation of contraction; • negative regulation of transforming growth factor beta receptor signaling pathway; • protein localization to basolateral plasma membrane; • receptor internalization involved in canonical Wnt signaling pathway; • regulation of membrane repolarization during action potential; • positive regulation of peptidyl-serine phosphorylation; • negative regulation of protein tyrosine kinase activity; • regulation of entry of bacterium into host cell; • مپ کیناز; • positive regulation of vasoconstriction; • negative regulation of potassium ion transmembrane transport; • lactation; • receptor-mediated endocytosis of virus by host cell; • regulation of blood coagulation; • regulation of ventricular cardiac muscle cell action potential; • protein homooligomerization; • GO:0022415 viral process; • positive regulation of intrinsic apoptotic signaling pathway; • negative regulation of receptor signaling pathway via JAK-STAT; • mammary gland involution; • calcium ion homeostasis; • negative regulation of necroptotic process; • regulation of the force of heart contraction; • lipid storage; • nitric oxide homeostasis; • membrane depolarization; • negative regulation of cytokine-mediated signaling pathway; • cellular calcium ion homeostasis; • GO:1901227 negative regulation of transcription by RNA polymerase II; • response to estrogen; • response to calcium ion; • regulation of fatty acid metabolic process; • cellular response to exogenous dsRNA; • negative regulation of MAPK cascade; • regulation of ruffle assembly; • positive regulation of protein binding; • positive regulation of protein ubiquitination; • negative regulation of anoikis; • leukocyte migration; • GO:0034613 protein localization; • positive regulation of cell adhesion molecule production; • response to hypoxia; • negative regulation of nitric-oxide synthase activity; • response to bacterium; • caveola assembly; • cellular response to hyperoxia; • cholesterol transport; • cellular response to starvation; • T cell costimulation; • regulation of nitric-oxide synthase activity; • receptor internalization; • positive regulation of peptidase activity; • positive regulation of ER-associated ubiquitin-dependent protein catabolic process; • negative regulation of endothelial cell proliferation; • negative regulation of BMP signaling pathway; • negative regulation of protein ubiquitination; • cellular response to peptide hormone stimulus; • GO:1901313 positive regulation of gene expression; • negative regulation of nitric oxide biosynthetic process; • angiotensin-activated signaling pathway involved in heart process; • protein complex oligomerization; • negative regulation of peptidyl-serine phosphorylation; • posttranscriptional regulation of gene expression; • positive regulation of gap junction assembly; • maintenance of protein location in cell; • negative regulation of signal transduction; • regulation of the force of heart contraction by chemical signal; • regulation of cell communication by electrical coupling involved in cardiac conduction; • regulation of heart rate by cardiac conduction; • negative regulation of epithelial cell differentiation; • skeletal muscle tissue development; • beta-catenin destruction complex disassembly; • GO:0048554 positive regulation of catalytic activity; • positive regulation of canonical Wnt signaling pathway; • negative regulation of tyrosine phosphorylation of STAT protein; • negative regulation of inward rectifier potassium channel activity; • دگرگونی یاخته‌; • positive regulation of cell migration; • positive regulation of cold-induced thermogenesis; • positive regulation of NF-kappaB transcription factor activity;
	منابع: آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
	857
	12389
	ENSG00000105974
	ENSMUSG00000007655
	Q03135
	P49817
	NM_001172895، NM_001172896، NM_001172897 NM_001753، NM_001172895، NM_001172896، NM_001172897
	NM_007616، XM_006504974، XM_006504975، XM_006504976 NM_001243064، NM_007616، XM_006504974، XM_006504975، XM_006504976
	NP_001166367، NP_001166368، NP_001744 NP_001166366، NP_001166367، NP_001166368، NP_001744
	NP_031642، XP_006505037، XP_006505038، XP_006505039 NP_001229993، NP_031642، XP_006505037، XP_006505038، XP_006505039
	ویکی‌داده
مشاهده/ویرایش انسان	مشاهده/ویرایش موش

کاویئولین ۱ (به انگلیسی: Caveolin 1) یک پروتئین است که در انسان توسط ژن «CAV1» واقع بر بازوی بلند کروموزوم ۷ کُدگذاری می‌شود.^[۴]

این پروتئین داربستی مهمترین بخش سازندهٔ حفره غشایی است و احتمالاً نقش سرکوب‌گر تومور را نیز می‌تواند ایفا کند.

کاویئولین ۱ با مولکول‌های تیروزین-پروتئین کیناز CSK، کلسترول،^[۵] گیرنده آندروژن،^[۶] گیرنده فاکتور رشد اپیدرمی،^[۷] گیرنده اندوتلین بی،^[۸] TRAF2،^[۹]^[۱۰] کاویئولین ۲^[۱۱]^[۱۲] و SCP2^[۱۳] تعامل پروتئین-پروتئین دارد.

منابع

↑ ^۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000007655 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R (March 1999). "Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors". Genomics. 56 (3): 355–6. doi:10.1006/geno.1998.5723. PMID 10087206.
↑ Li S, Song KS, Lisanti MP (January 1996). "Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes". The Journal of Biological Chemistry. 271 (1): 568–73. doi:10.1074/jbc.271.1.568. PMID 8550621.
↑ Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP (April 2001). "Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation". The Journal of Biological Chemistry. 276 (16): 13442–51. doi:10.1074/jbc.M006598200. PMID 11278309.
↑ Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities". The Journal of Biological Chemistry. 272 (48): 30429–38. doi:10.1074/jbc.272.48.30429. PMID 9374534.
↑ Yamaguchi T, Murata Y, Fujiyoshi Y, Doi T (April 2003). "Regulated interaction of endothelin B receptor with caveolin-1". European Journal of Biochemistry. 270 (8): 1816–27. doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195.
↑ Feng X, Gaeta ML, Madge LA, Yang JH, Bradley JR, Pober JS (March 2001). "Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors". The Journal of Biological Chemistry. 276 (11): 8341–9. doi:10.1074/jbc.M007116200. PMID 11112773.
↑ Cao H, Courchesne WE, Mastick CC (March 2002). "A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase". The Journal of Biological Chemistry. 277 (11): 8771–4. doi:10.1074/jbc.C100661200. PMID 11805080.
↑ Breuza L, Corby S, Arsanto JP, Delgrossi MH, Scheiffele P, Le Bivic A (December 2002). "The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells". Journal of Cell Science. 115 (Pt 23): 4457–67. doi:10.1242/jcs.00130. PMID 12414992.
↑ Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, Kohtz DS, van Donselaar E, Peters P, Lisanti MP (November 1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". The Journal of Biological Chemistry. 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. PMID 9361015.
↑ Zhou M, Parr RD, Petrescu AD, Payne HR, Atshaves BP, Kier AB, Ball JM, Schroeder F (June 2004). "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry. 43 (23): 7288–306. doi:10.1021/bi035914n. PMID 15182174.

مشارکت‌کنندگان ویکی‌پدیا. «Caveolin 1». در دانشنامهٔ ویکی‌پدیای انگلیسی.

برای مطالعهٔ بیشتر

Engelman JA, Zhang X, Galbiati F, Volonte D, Sotgia F, Pestell RG, Minetti C, Scherer PE, Okamoto T, Lisanti MP (December 1998). "Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy". American Journal of Human Genetics. 63 (6): 1578–87. doi:10.1086/302172. PMC 1377628. PMID 9837809.
Razani B, Schlegel A, Liu J, Lisanti MP (August 2001). "Caveolin-1, a putative tumour suppressor gene". Biochemical Society Transactions. 29 (Pt 4): 494–9. doi:10.1042/BST0290494. PMID 11498016.
Fujimoto T, Kogo H, Nakamura N, Ozeki S (March 2002). "[Microdomains and caveolin]". Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47 (4 Suppl): 326–32. PMID 11915322.
Shatz M, Liscovitch M (September 2004). "Caveolin-1 and cancer multidrug resistance: coordinate regulation of pro-survival proteins?". Leukemia Research. 28 (9): 907–8. doi:10.1016/j.leukres.2004.03.013. PMID 15234566.
Frank PG, Lisanti MP (January 2007). "Caveolin-1 and liver regeneration: role in proliferation and lipogenesis". Cell Cycle. 6 (2): 115–6. doi:10.4161/cc.6.2.3722. PMID 17314510.

این یک مقالهٔ خرد زیست‌شناسی مولکولی است. می‌توانید با گسترش آن به ویکی‌پدیا کمک کنید.

[refGRCm38Ensembl-1] ۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000007655 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10087206-4] Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R (March 1999). "Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors". Genomics. 56 (3): 355–6. doi:10.1006/geno.1998.5723. PMID 10087206.

[5] Li S, Song KS, Lisanti MP (January 1996). "Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes". The Journal of Biological Chemistry. 271 (1): 568–73. doi:10.1074/jbc.271.1.568. PMID 8550621.

[pmid11278309-6] Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP (April 2001). "Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation". The Journal of Biological Chemistry. 276 (16): 13442–51. doi:10.1074/jbc.M006598200. PMID 11278309.

[pmid9374534-7] Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities". The Journal of Biological Chemistry. 272 (48): 30429–38. doi:10.1074/jbc.272.48.30429. PMID 9374534.

[pmid12694195-8] Yamaguchi T, Murata Y, Fujiyoshi Y, Doi T (April 2003). "Regulated interaction of endothelin B receptor with caveolin-1". European Journal of Biochemistry. 270 (8): 1816–27. doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195.

[pmid11112773-9] Feng X, Gaeta ML, Madge LA, Yang JH, Bradley JR, Pober JS (March 2001). "Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors". The Journal of Biological Chemistry. 276 (11): 8341–9. doi:10.1074/jbc.M007116200. PMID 11112773.

[pmid11805080-10] Cao H, Courchesne WE, Mastick CC (March 2002). "A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase". The Journal of Biological Chemistry. 277 (11): 8771–4. doi:10.1074/jbc.C100661200. PMID 11805080.

[pmid12414992-11] Breuza L, Corby S, Arsanto JP, Delgrossi MH, Scheiffele P, Le Bivic A (December 2002). "The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells". Journal of Cell Science. 115 (Pt 23): 4457–67. doi:10.1242/jcs.00130. PMID 12414992.

[pmid9361015-12] Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, Kohtz DS, van Donselaar E, Peters P, Lisanti MP (November 1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". The Journal of Biological Chemistry. 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. PMID 9361015.

[pmid15182174-13] Zhou M, Parr RD, Petrescu AD, Payne HR, Atshaves BP, Kier AB, Ball JM, Schroeder F (June 2004). "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry. 43 (23): 7288–306. doi:10.1021/bi035914n. PMID 15182174.

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